PDBsum entry: 2k1j

Gene regulation

PDB-id

2k1j

Contents

Description

Header details

Protein chain

Metal ions

_ZN ×2

* Residue conservation analysis

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PDB id:

2k1j

Name:

Gene regulation

Title:

Plan homeodomain finger of tumour supressor ing4

Structure:

Inhibitor of growth protein 4. Chain: a. Fragment: phd-type zinc-finger, unp residues 188-249. Synonym: p29ing4. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: ing4. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.

UniProt:

Q9UNL4 (ING4_HUMAN)

Seq:

249 a.a.

Struc:

63 a.a.*

Key:		PfamA domain			PfamB domain
		Secondary structure

* PDB and UniProt seqs differ at 1 residue position (black cross)

Resolution:

not givenÅ

NMR structure:

25 models

Authors:

A.Palacios,P.Garcia,D.Padro,E.Lopez-Hernandez,F.J.Blanco

Key ref:

A.Palacios et al. (2006). Solution structure and NMR characterization of the binding to methylated histone tails of the plant homeodomain finger of the tumour suppressor ING4.. Febs Lett, 580, 6903-6908. [PubMed id: 17157298] [DOI: 10.1016/j.febslet.2006.11.055]

Date:

05-Mar-08

Release date:

15-Apr-08

Supersedes:

2jmq

Related entries:

7210 related db: bmrb

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Key reference

DOI no: 10.1016/j.febslet.2006.11.055 Febs Lett 580:6903-6908 (2006)

PubMed id: 17157298

Solution structure and NMR characterization of the binding to methylated histone tails of the plant homeodomain finger of the tumour suppressor ING4.

A.Palacios, P.Garcia, D.Padró, E.López-Hernández, I.Martín, F.J.Blanco.

ABSTRACT

Plant homeodomain (PHD) fingers are frequently present in proteins involved in chromatin remodelling, and some of them bind to histones. The family of proteins inhibitors of growth (ING) contains a PHD finger that bind to histone-3 trimethylated at lysine 4, and those of ING1 and ING2 also act as nuclear phosphoinositide receptors. We have determined the structure of ING4 PHD, and characterised its binding to phosphoinositides and histone methylated tails. In contrast to ING2, ING4 is not a phosphoinositide receptor and binds with similar affinity to the different methylation states of histone-3 at lysine 4.

Literature references that cite this PDB file's key reference

PubMed id Reference

19015549 J.Luo, S.Shah, K.Riabowol, and P.E.Mains (2009).
The Caenorhabditis elegans ing-3 gene regulates ionizing radiation-induced germ-cell apoptosis in a p53-associated pathway.

Genetics, 181, 473-482.

19432890 M.Unoki, K.Kumamoto, S.Takenoshita, and C.C.Harris (2009).
Reviewing the current classification of inhibitor of growth family proteins.

Cancer Sci, 100, 1173-1179.

18381289 A.Palacios, I.G.Muñoz, D.Pantoja-Uceda, M.J.Marcaida, D.Torres, J.M.Martín-García, I.Luque, G.Montoya, and F.J.Blanco (2008).
Molecular basis of histone H3K4me3 recognition by ING4.

J Biol Chem, 283, 15956-15964.

PDB code: 2vnf

18691180 M.A.Soliman, P.Berardi, S.Pastyryeva, P.Bonnefin, X.Feng, A.Colina, D.Young, and K.Riabowol (2008).
ING1a expression increases during replicative senescence and induces a senescent phenotype.

Aging Cell, 7, 783-794.

18794358 M.Ullah, N.Pelletier, L.Xiao, S.P.Zhao, K.Wang, C.Degerny, S.Tahmasebi, C.Cayrou, Y.Doyon, S.L.Goh, N.Champagne, J.Côté, and X.J.Yang (2008).
Molecular architecture of quartet MOZ/MORF histone acetyltransferase complexes.

Mol Cell Biol, 28, 6828-6843.

18779315 S.Nozell, T.Laver, D.Moseley, L.Nowoslawski, M.De Vos, G.P.Atkinson, K.Harrison, L.B.Nabors, and E.N.Benveniste (2008).
The ING4 tumor suppressor attenuates NF-kappaB activity at the promoters of target genes.

Mol Cell Biol, 28, 6632-6645.

18836436 X.Han, X.Feng, J.B.Rattner, H.Smith, P.Bose, K.Suzuki, M.A.Soliman, M.S.Scott, B.E.Burke, and K.Riabowol (2008).
Tethering by lamin A stabilizes and targets the ING1 tumour suppressor.

Nat Cell Biol, 10, 1333-1340.

17693408 M.Abad, C.Menéndez, A.Füchtbauer, M.Serrano, E.M.Füchtbauer, and I.Palmero (2007).
Ing1 mediates p53 accumulation and chromatin modification in response to oncogenic stress.

J Biol Chem, 282, 31060-31067.

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.